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Methionine aminopeptidase (EC 3.4.11.18) (Fragment)

 Q862K9_BOVIN            Unreviewed;       189 AA.
Q862K9;
01-JUN-2003, integrated into UniProtKB/TrEMBL.
01-JUN-2003, sequence version 1.
05-JUL-2017, entry version 83.
RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
Flags: Fragment;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913 {ECO:0000313|EMBL:BAC56465.1};
[1] {ECO:0000313|EMBL:BAC56465.1}
NUCLEOTIDE SEQUENCE.
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
-!- FUNCTION: Removes the N-terminal methionine from nascent proteins.
The N-terminal methionine is often cleaved when the second residue
in the primary sequence is small and uncharged (Met-Ala-, Cys,
Gly, Pro, Ser, Thr, or Val). {ECO:0000256|RuleBase:RU003653}.
-!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
preferentially methionine, from peptides and arylamides.
{ECO:0000256|RuleBase:RU003653, ECO:0000256|SAAS:SAAS00684747}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000256|RuleBase:RU003653};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|RuleBase:RU003653};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|RuleBase:RU003653};
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000256|RuleBase:RU003653};
Note=Binds 2 divalent metal cations per subunit. Has a high-
affinity and a low affinity metal-binding site. The true nature of
the physiological cofactor is under debate. The enzyme is active
with cobalt, zinc, manganese or divalent iron ions. Most likely,
methionine aminopeptidases function as mononuclear Fe(2+)-
metalloproteases under physiological conditions, and the
catalytically relevant metal-binding site has been assigned to the
histidine-containing high-affinity site.
{ECO:0000256|RuleBase:RU003653};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000256|SAAS:SAAS00684757};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|SAAS:SAAS00684758};
-!- SIMILARITY: Belongs to the peptidase M24A family.
{ECO:0000256|RuleBase:RU003653}.
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EMBL; AB098975; BAC56465.1; -; mRNA.
UniGene; Bt.49424; -.
ProteinModelPortal; Q862K9; -.
PaxDb; Q862K9; -.
eggNOG; KOG2775; Eukaryota.
eggNOG; COG0024; LUCA.
GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
InterPro; IPR000994; Pept_M24.
InterPro; IPR001714; Pept_M24_MAP.
InterPro; IPR002468; Pept_M24A_MAP2.
InterPro; IPR018349; Pept_M24A_MAP2_BS.
Pfam; PF00557; Peptidase_M24; 1.
PRINTS; PR00599; MAPEPTIDASE.
SUPFAM; SSF55920; SSF55920; 1.
TIGRFAMs; TIGR00501; met_pdase_II; 1.
PROSITE; PS01202; MAP_2; 1.
2: Evidence at transcript level;
Aminopeptidase {ECO:0000256|RuleBase:RU003653,
ECO:0000256|SAAS:SAAS00684759, ECO:0000313|EMBL:BAC56465.1};
Hydrolase {ECO:0000256|RuleBase:RU003653,
ECO:0000256|SAAS:SAAS00684759, ECO:0000313|EMBL:BAC56465.1};
Metal-binding {ECO:0000256|RuleBase:RU003653,
ECO:0000256|SAAS:SAAS00684750};
Protease {ECO:0000256|RuleBase:RU003653,
ECO:0000256|SAAS:SAAS00684759, ECO:0000313|EMBL:BAC56465.1}.
DOMAIN 10 173 Peptidase_M24.
{ECO:0000259|Pfam:PF00557}.
NON_TER 1 1 {ECO:0000313|EMBL:BAC56465.1}.
NON_TER 189 189 {ECO:0000313|EMBL:BAC56465.1}.
SEQUENCE 189 AA; 20645 MW; 0B0BCC55D6EA269B CRC64;
KLEDCSRKLI KENGLNAGLA FPTGCSLNNC AAHYTPNAGD TTVLQYDDIC KIDFGTHISG
RIIDCAFTVT FNPKYDTLLK AVKDATNTGI KCAGIDVRLC DVGEAIQEVM ESYEVEIDGK
TYQVKPIRNL NGHSIGPYRI HAGKTVPIVK GGEATRMEEG EVYAIETFGS TGKGVVHDDM
ECSHYMNKF


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